1QTR

CRYSTAL STRUCTURE ANALYSIS OF THE PROLYL AMINOPEPTIDASE FROM SERRATIA MARCESCENS

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	293
Detector technology	IMAGE PLATE
Collection date	1997-10-25
Detector	RIGAKU RAXIS IIC
Spacegroup name	P 43 21 2
Unit cell lengths	65.360, 65.360, 169.200
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	8.000 - 2.320
R-factor	0.189
Rwork	0.189
R-free	0.26700
RMSD bond length	0.009 *
RMSD bond angle	1.390 *
Phasing software	DM
Refinement software	X-PLOR

Data quality characteristics

	Overall
Low resolution limit [Å]	10.000
High resolution limit [Å]	2.320
Rmerge	0.059
Total number of observations	45646 *
Number of reflections	14917 *
Completeness [%]	89.1

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	20 *	Kabashima, T., (1997) J.Biochem.(Tokyo), 122, 601. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	28 (mg/ml)
2	1	reservoir	Na-cacodylate	0.1 (M)
3	1	reservoir	Na acetate	0.2 (M)
4	1	reservoir	PEG6000	20 (%)